Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilization.
about
Stabilization of a protein conferred by an increase in folded state entropyThe intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli.Drosophila melanogaster acylphosphatase: a common ancestor for acylphosphatase isoenzymes of vertebrate species.Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.Development of Enzymatic Activity during Protein Folding
P2860
Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilization.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Structural and kinetic investi ...... conformational stabilization.
@en
type
label
Structural and kinetic investi ...... conformational stabilization.
@en
prefLabel
Structural and kinetic investi ...... conformational stabilization.
@en
P2093
P50
P356
P1433
P1476
Structural and kinetic investi ...... d conformational stabilization
@en
P2093
Nordlund P
Thunnissen MM
P304
P356
10.1021/BI970173+
P407
P577
1997-06-01T00:00:00Z